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Protein

Isoaspartyl peptidase/L-asparaginase

Gene
N/A
Organism
Lupinus luteus (European yellow lupine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Also has L-asparaginase activity, which is used to liberate stored nitrogen during seed development.

Catalytic activityi

Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.

Kineticsi

No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln or aspartylglucosamides.
  1. KM=0.136 mM for beta-L-Asp-L-Leu1 Publication
  2. KM=4.8 mM for L-Asn1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei193NucleophileBy similarity1

    GO - Molecular functioni

    Keywordsi

    Molecular functionHydrolase, Protease

    Enzyme and pathway databases

    SABIO-RKiQ9ZSD6.

    Protein family/group databases

    MEROPSiT02.A01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5)
    Short name:
    LlA
    Alternative name(s):
    L-asparagine amidohydrolase
    Potassium-independent L-asparaginase
    Cleaved into the following 2 chains:
    OrganismiLupinus luteus (European yellow lupine)
    Taxonomic identifieri3873 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000454561 – 192Isoaspartyl peptidase/L-asparaginase subunit alphaAdd BLAST192
    ChainiPRO_0000045457193 – 325Isoaspartyl peptidase/L-asparaginase subunit betaAdd BLAST133

    Post-translational modificationi

    Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei192 – 193Cleavage; by autolysis2

    Keywords - PTMi

    Autocatalytic cleavage

    Expressioni

    Tissue specificityi

    Expressed in ripening seeds and developing nodules.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.1 Publication

    Structurei

    Secondary structure

    1325
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 13Combined sources9
    Helixi21 – 43Combined sources23
    Helixi48 – 61Combined sources14
    Beta strandi65 – 68Combined sources4
    Beta strandi81 – 87Combined sources7
    Turni88 – 91Combined sources4
    Beta strandi92 – 103Combined sources12
    Helixi105 – 115Combined sources11
    Beta strandi119 – 122Combined sources4
    Helixi123 – 133Combined sources11
    Helixi140 – 143Combined sources4
    Helixi146 – 158Combined sources13
    Beta strandi194 – 199Combined sources6
    Beta strandi205 – 211Combined sources7
    Turni229 – 231Combined sources3
    Beta strandi232 – 234Combined sources3
    Beta strandi236 – 244Combined sources9
    Helixi246 – 251Combined sources6
    Helixi254 – 265Combined sources12
    Helixi269 – 278Combined sources10
    Beta strandi285 – 292Combined sources8
    Beta strandi301 – 312Combined sources12
    Beta strandi317 – 322Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GEZX-ray2.60A/C/E/G1-192[»]
    B/D/F/H193-325[»]
    ProteinModelPortaliQ9ZSD6.
    SMRiQ9ZSD6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZSD6.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni221 – 224Substrate bindingBy similarity4
    Regioni243 – 246Substrate bindingBy similarity4

    Sequence similaritiesi

    Belongs to the Ntn-hydrolase family.Curated

    Family and domain databases

    InterProiView protein in InterPro
    IPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    PANTHERiPTHR10188. PTHR10188. 1 hit.
    PfamiView protein in Pfam
    PF01112. Asparaginase_2. 1 hit.
    SUPFAMiSSF56235. SSF56235. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9ZSD6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGGWSIALHG GAGDIPFSLP PERRKPREEG LRHCLQIGVE ALKAQKPPLD
    60 70 80 90 100
    VVELVVRELE NIEHFNAGIG SVLTNSGTVE MEASIMDGNT MKCGAVSGLS
    110 120 130 140 150
    TVLNPISLAR LVMDKTPHIY LAFQGAQDFA KQQGVETVDS SHLITAENVE
    160 170 180 190 200
    RLKLAIEANR VQVDYSQYNY PEPVKDDAEK ELPLTNGDSQ IGTVGCVAVD
    210 220 230 240 250
    SHGNLASATS TGGLVNKMVG RIGDTPLIGA GTYANELCAV SATGKGEEII
    260 270 280 290 300
    RATVARDVAA LMEFKGLSLK EAADFVIHER TPKGTVGLIA VSAAGEIAMP
    310 320
    FNTTGMFRAC ATEDGYSEIA IWPTT
    Length:325
    Mass (Da):34,449
    Last modified:May 1, 1999 - v1
    Checksum:i52949AA1765B7892
    GO

    Mass spectrometryi

    Molecular mass is 22983 Da from positions 1 - 192. Determined by ESI. Subunit alpha overexpressed as a His-tagged protein where the His tag has the mass 2050.1 Publication
    Molecular mass is 13605 Da from positions 193 - 325. Determined by ESI. Subunit beta.1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF112444 mRNA. Translation: AAD03742.1.

    Similar proteinsi

    Entry informationi

    Entry nameiASPG_LUPLU
    AccessioniPrimary (citable) accession number: Q9ZSD6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: April 12, 2017
    This is version 74 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families